Analytical Data
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Gene name
PRDM2
- Application
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Alternative Names
PRDM2；KMT8；RIZ；PR domain zinc finger Protein 2
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q13029
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Expression Region
全长
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AA Sequence
full
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
PRDM2, also known as PRDI-BF1 (Positive Regulatory Domain I-Binding Factor 1), is a member of the PRDM (PRDI-BF1 and RIZ1 homologous domain) family of proteins that play critical roles in various biological processes, including gene regulation, cellular differentiation, and development. PRDM2 functions as a transcriptional regulator, influencing the expression of numerous genes involved in immune responses and tumor suppression. Dysregulation of PRDM2 has been implicated in several types of cancer, making it a significant focus for research aimed at understanding its role in tumor biology. Specifically, the study of PRDM2 recombinant proteins allows scientists to investigate the structure-function relationships of this protein, enabling insights into its interactions with DNA and other cellular partners. These studies can provide valuable information about its regulatory mechanisms, potential as a therapeutic target, and its involvement in disease states. As recombinant technology advances, generating PRDM2 proteins for detailed biochemical analysis and functional assays becomes more accessible, paving the way for innovative approaches in cancer therapy and other fields. This research underscores the importance of PRDM2 in maintaining cellular homeostasis and its potential as a biomarker for disease progression.
